Table 1.
Data collection and refinement statistics
| D2A6, M.HhaI(T250G)–APtarget–AdoHcy | D75A6, M.HhaI–APadj–AdoHcy | 2D2, M.HhaI–APopp–AdoHcy | D80A2, M.HhaI–APout–AdoHcy | |
|---|---|---|---|---|
| Data collection | ||||
| Space group | H32 | H32 | H32 | H32 |
| Cell dimensions | ||||
| a, b, c (Å) | 95.6, 95.6, 315.8 | 95.1, 95.1, 312.2 | ||
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
| Resolution (Å) | 29.5–1.9 (2.00–1.90)a | 23.2–1.9 (1.95–1.90) | 56.8–1.7 (1.79–1.70) | 31.0–1.85 (1.96–1.85) |
| Rmerge (%) | 6.7 (23.9) | 5.0 (22.0) | 7.1 (33.9) | 6.7 (20.4) |
| I/σI | 8.4 (2.8) | 30.0 (18.4) | 7.5 (2.2) | 8.5 (3.7) |
| Completeness (%) | 99.9 (99.6) | 99.4 (97.4) | 99.6 (97.6) | 98.7 (94.5) |
| Redundancy | 6.0 (6.0) | 17.4 (16.6) | 11.8 (7.5) | 8.7 (3.6) |
| Refinement | ||||
| Resolution (Å) | 1.90 | 1.90 | 1.70 | 1.85 |
| No. reflections | 44234 | 43361 | 59771 | 45796 |
| Rwork/Rfree | 20.0 (23.7)/21.9 (24.5) | 19.4 (21.7)/21.5 (22.7) | 19.6 (24.8)/22.0 (25.1) | 18.9 (21.3)/21.2 (23.7) |
| Coordinate error (Å) | 0.17 | 0.14 | 0.14 | 0.14 |
| No. of atoms | 3389 | 3549 | 3380 | 3585 |
| Ligand/ion | 566 | 572 | 573 | 588 |
| Water | 220 | 342 | 186 | 376 |
| B-factors | ||||
| Protein | 16.3 | 15.9 | 16.5 | 13.1 |
| Ligand/ion | 27.2 | 25.9 | 25.3 | 23.3 |
| Water | 25.2 | 29.9 | 22.1 | 25.4 |
| R.m.s deviations | ||||
| Bond lengths (Å) | 0.006 | 0.006 | 0.006 | 0.006 |
| Bond angles (degrees) | 1.2 | 1.3 | 1.2 | 1.3 |
Wavelengths used for data collection: D2A6 (λ = 0.9755 Å, T = 100 K, detector MarCCD, beamline ID13, ESRF, Grenoble); D75A6 (λ = 0.8120 Å, T = 100 K, detector Mar345, beamline DORIS/X11, EMBL-DESY, Hamburg); 2D2 (λ = 0.8120 Å, T = 100 K, detector MarCCD, beamline DORIS/X11, EMBL-DESY, Hamburg); D80A2 (λ = 1.050 Å, T = 100 K, detector Mar345, beamline DORIS/X31, EMBL-DESY, Hamburg).
aHighest resolution shell is shown in parentheses.